Triplet-triplet energy transfer (TTET) between xanthone and naphthalene was used to investigate end-to-end loop formation in unfolded polypeptide chains and to study the influence of additional tails on the dynamics. Furthermore, we examined β-turn formation in short model peptides. At last, we wanted to study the dynamics in the unfolded state of a full-length protein. Therefore, we established a method that allowed for the site-specific incorporation of TTET labels into proteins using unnatural amino acids and bioorthogonal chemistry.
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Triplet-triplet energy transfer (TTET) between xanthone and naphthalene was used to investigate end-to-end loop formation in unfolded polypeptide chains and to study the influence of additional tails on the dynamics. Furthermore, we examined β-turn formation in short model peptides. At last, we wanted to study the dynamics in the unfolded state of a full-length protein. Therefore, we established a method that allowed for the site-specific incorporation of TTET labels into proteins using unnatura...
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